The Amino Acid at Position 8 of the Proteolytic Cleavage Site of the Mumps Virus Fusion Protein Affects Viral Proteolysis and Fusogenicity.

ABSTRACT: The mumps virus (MuV) fusion protein (F) plays a crucial role for the entry process and spread of infection by mediating fusion between viral and cellular membranes as well as between infected and neighboring cells, respectively. The fusogenicity of MuV differs depending on the strain and might correlate with the virulence; however, it is unclear which mechanisms contribute to the differentiated fusogenicity. The cleavage motif of MuV F is highly conserved among all strains, except the amino acid residue at position 8 (P8) that shows a certain variability with a total of four amino acid variants (leucine [L], proline [P], serine [S], and threonine [T]). We demonstrate that P8 affects the proteolytic processing and the fusogenicity of MuV F. The presence of L or S at P8 resulted in a slower

SUBMITTER: Huttl S 

PROVIDER: S-EPMC7592220 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature